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Turning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations
- Bogdanov, Alexey
M., Acharya, Atanu, Titelmayer, Anastasia V., Mamontova, Anastasia V., Bravaya, Ksenia B., Kolomeisky, Anatoly B., Lukyanov, Konstantin A., Krylov, Anna I.
- Journal of the American Chemical Society 2016 v.138 no.14 pp. 4807-4817
- electron transfer, fluorescent proteins, mutants, photooxidation, photostability, point mutation
- Photoinduced electron transfer in fluorescent proteins from the GFP family can be regarded either as an asset facilitating new applications or as a nuisance leading to the loss of optical output. Photooxidation commonly results in green-to-red photoconversion called oxidative redding. We discovered that yellow FPs do not undergo redding; however, the redding is restored upon halide binding. Calculations of the energetics of one-electron oxidation and possible electron transfer (ET) pathways suggested that excited-state ET proceeds through a hopping mechanism via Tyr145. In YFPs, the π-stacking of the chromophore with Tyr203 reduces its electron-donating ability, which can be restored by halide binding. Point mutations confirmed that Tyr145 is a key residue controlling ET. Substitution of Tyr145 by less-efficient electron acceptors resulted in highly photostable mutants. This strategy (i.e., calculation and disruption of ET pathways by mutations) may represent a new approach toward enhancing photostability of FPs.